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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Phosphorylation of LRRK2 by casein kinase 1α regulates trans-Golgi clustering via differential interaction with ARHGEF7
Ruth Chia, Sara Haddock, Alexandra Beilina, et al.
Nature Communications (2014) Vol. 5, Iss. 1
Open Access | Times Cited: 95

Showing 26-50 of 95 citing articles:

Binding of the Human 14-3-3 Isoforms to Distinct Sites in the Leucine-Rich Repeat Kinase 2
Jascha T. Manschwetus, Maximilian Wallbott, Alexandra Fachinger, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 54
LRRK2 Phosphorylation, More Than an Epiphenomenon
Antoine Marchand, Matthieu Drouyer, Alessia Sarchione, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 52
Impact of Type II LRRK2 inhibitors on signaling and mitophagy
Anna Tasegian, François Singh, Ian G. Ganley, et al.
Biochemical Journal (2021) Vol. 478, Iss. 19, pp. 3555-3573
Open Access | Times Cited: 51
LncRNA XIST sponges miR-199a-3p to modulate the Sp1/LRRK2 signal pathway to accelerate Parkinson’s disease progression
Qian Zhou, Mingming Zhang, Min Liu, et al.
Aging (2021) Vol. 13, Iss. 3, pp. 4115-4137
Open Access | Times Cited: 41
Understanding the GTPase Activity of LRRK2: Regulation, Function, and Neurotoxicity
An Phu Tran Nguyen, Darren J. Moore
Advances in neurobiology (2017), pp. 71-88
Open Access | Times Cited: 56
Proteomic analysis reveals co-ordinated alterations in protein synthesis and degradation pathways in LRRK2 knockout mice
Laura Pellegrini, David N. Hauser, Yan Li, et al.
Human Molecular Genetics (2018) Vol. 27, Iss. 18, pp. 3257-3271
Open Access | Times Cited: 55
LRRK2 inhibitors and their potential in the treatment of Parkinson’s disease: current perspectives
Farzaneh Atashrazm, Nicolas Dzamko
Clinical Pharmacology Advances and Applications (2016) Vol. Volume 8, pp. 177-189
Open Access | Times Cited: 53
Lrrk promotes tau neurotoxicity through dysregulation of actin and mitochondrial dynamics
Farah H. Bardai, Dalila G. Ordonez, Rachel M. Bailey, et al.
PLoS Biology (2018) Vol. 16, Iss. 12, pp. e2006265-e2006265
Open Access | Times Cited: 53
Pathogenic LRRK2 variants are gain-of-function mutations that enhance LRRK2-mediated repression of β-catenin signaling
Daniel C. Berwick, Behzâd Javaheri, Andrea Wetzel, et al.
Molecular Neurodegeneration (2017) Vol. 12, Iss. 1
Open Access | Times Cited: 50
PAK6 Phosphorylates 14-3-3γ to Regulate Steady State Phosphorylation of LRRK2
Laura Civiero, Susanna Cogo, Anneleen Kiekens, et al.
Frontiers in Molecular Neuroscience (2017) Vol. 10
Open Access | Times Cited: 50
Recent Developments in LRRK2-Targeted Therapy for Parkinson’s Disease
Ye Zhao, Nicolas Dzamko
Drugs (2019) Vol. 79, Iss. 10, pp. 1037-1051
Closed Access | Times Cited: 50
Clinically Precedented Protein Kinases: Rationale for Their Use in Neurodegenerative Disease
Caroline Benn, Lee A. Dawson
Frontiers in Aging Neuroscience (2020) Vol. 12
Open Access | Times Cited: 42
Pathways to Parkinson’s disease: a spotlight on 14-3-3 proteins
Elena Giusto, Talene A. Yacoubian, Elisa Greggio, et al.
npj Parkinson s Disease (2021) Vol. 7, Iss. 1
Open Access | Times Cited: 39
The LRRK2 signalling system
Alice Price, Claudia Manzoni, Mark Cookson, et al.
Cell and Tissue Research (2018) Vol. 373, Iss. 1, pp. 39-50
Open Access | Times Cited: 43
The Current State-of-the Art of LRRK2-Based Biomarker Assay Development in Parkinson’s Disease
Hardy J. Rideout, Marie‐Christine Chartier‐Harlin, Matthew Fell, et al.
Frontiers in Neuroscience (2020) Vol. 14
Open Access | Times Cited: 39
Leucine-rich repeat kinase-2 (LRRK2) modulates microglial phenotype and dopaminergic neurodegeneration
Zach Dwyer, Chris Rudyk, Ashley Thompson, et al.
Neurobiology of Aging (2020) Vol. 91, pp. 45-55
Open Access | Times Cited: 38
Sequential screening nominates the Parkinson's disease associated kinase LRRK2 as a regulator of Clathrin-mediated endocytosis
George R. Heaton, Natalie Landeck, Adamantios Mamais, et al.
Neurobiology of Disease (2020) Vol. 141, pp. 104948-104948
Open Access | Times Cited: 34
The Regulation of Rab GTPases by Phosphorylation
Lejia Xu, Yuki Nagai, Yotaro Kajihara, et al.
Biomolecules (2021) Vol. 11, Iss. 9, pp. 1340-1340
Open Access | Times Cited: 28
The Roc domain of LRRK2 as a hub for protein-protein interactions: a focus on PAK6 and its impact on RAB phosphorylation
Susanna Cogo, Franz Y. Ho, Elena Tosoni, et al.
Brain Research (2022) Vol. 1778, pp. 147781-147781
Open Access | Times Cited: 21
Genome-wide screen reveals Rab12 GTPase as a critical activator of pathogenic LRRK2 kinase
Herschel S. Dhekne, Francesca Tonelli, Wondwossen M Yeshaw, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2023)
Open Access | Times Cited: 11
Cross-talk between LRRK2 and PKA: implication for Parkinson's disease?
Elisa Greggio, Luigi Bubacco, Isabella Russo
Biochemical Society Transactions (2017) Vol. 45, Iss. 1, pp. 261-267
Open Access | Times Cited: 34
LRRK2: Genetic mechanisms vs genetic subtypes
Ignacio Mata, Philippe A. Salles, Mario Cornejo‐Olivas, et al.
Handbook of clinical neurology (2023), pp. 133-154
Closed Access | Times Cited: 9
LRRK2 phosphorylation status and kinase activity regulate (macro)autophagy in a Rab8a/Rab10-dependent manner
Elżbieta Kania, Jaclyn S. Long, David G. McEwan, et al.
Cell Death and Disease (2023) Vol. 14, Iss. 7
Open Access | Times Cited: 9
Leucine-rich repeat kinase 2 at a glance
Christiane Zhu, Susanne Herbst, Patrick A. Lewis
Journal of Cell Science (2023) Vol. 136, Iss. 17
Open Access | Times Cited: 9
The role of LRRK2 in cytoskeletal dynamics
Laura Civiero, Susanna Cogo, Alice Biosa, et al.
Biochemical Society Transactions (2018) Vol. 46, Iss. 6, pp. 1653-1663
Closed Access | Times Cited: 30

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